ELDP1_PINMA
ID ELDP1_PINMA Reviewed; 348 AA.
AC P86953;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 10-FEB-2021, entry version 19.
DE RecName: Full=EGF-like domain-containing protein 1;
DE Flags: Precursor; Fragment;
OS Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX NCBI_TaxID=104660;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC TISSUE=Mantle {ECO:0000269|PubMed:19915030};
RX PubMed=19915030; DOI=10.1093/molbev/msp278;
RA Jackson D.J., McDougall C., Woodcroft B., Moase P., Rose R.A., Kube M.,
RA Reinhardt R., Rokhsar D.S., Montagnani C., Joubert C., Piquemal D.,
RA Degnan B.M.;
RT "Parallel evolution of nacre building gene sets in molluscs.";
RL Mol. Biol. Evol. 27:591-608(2010).
RN [2]
RP PROTEIN SEQUENCE OF 32-55; 146-157 AND 187-215, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Shell;
RX PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT "Different secretory repertoires control the biomineralization processes of
RT prism and nacre deposition of the pearl oyster shell.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC Expressed primarily in the mantle with highest level in the mantle edge
CC and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC -!- SEQUENCE CAUTION:
CC Sequence=GT282449; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; GT278041; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT282449; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; GT284230; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; EZ420398; -; NOT_ANNOTATED_CDS; mRNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001507; ZP_dom.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..348
FT /note="EGF-like domain-containing protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000413070"
FT DOMAIN 60..92
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 99..342
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT DISULFID 64..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 68..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 82..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 159
FT /note="H -> R (in Ref. 1; GT278041)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="I -> M (in Ref. 1; EZ420398/GT278041)"
FT /evidence="ECO:0000305"
FT NON_TER 348
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38362 MW; 78A2C7C8035401AE CRC64;
MFYLSTFMTI VISLSLVSCS YDCNNPGYSC KGTCHYYGPC ICNEKLMGYD CSVLKSRMST
GSNCTVTCQN NGKCYDGSKC LCSSDYTGDL CEKQTTGARC TLDAVVFEAY RPIGFVGETY
LSQSRSCKLL ETTSDVPGMI KFERKIFHGD TSMCGLKKHM DIPSAGDVTY EADIYSTFQY
NSWGTRDFMD NVKCQYKPTR VGLSMDAPDS LFPIKMSARD GASSNVQATT QSAPISLLFS
PQNIPDVKGA MVDYLEVYSI NSTSKEYKSV VAVKNGCAQK NEYNVAFSNL DELDPATSKW
IGLVKMQAFI IFENEPILFN YRLRFCPDRC TTPTCAAPXV GQATSAAV